ID A0A0V1CED8_TRIBR Unreviewed; 855 AA.
AC A0A0V1CED8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Annulin {ECO:0000313|EMBL:KRY47600.1};
GN ORFNames=T03_12383 {ECO:0000313|EMBL:KRY47600.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY47600.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY47600.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY47600.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY47600.1}.
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DR EMBL; JYDI01000236; KRY47600.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CED8; -.
DR STRING; 45882.A0A0V1CED8; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.90.260.10; Transglutaminase-like; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR036985; Transglutaminase-like_sf.
DR InterPro; IPR023608; Transglutaminase_animal.
DR InterPro; IPR008958; Transglutaminase_C.
DR InterPro; IPR036238; Transglutaminase_C_sf.
DR InterPro; IPR001102; Transglutaminase_N.
DR PANTHER; PTHR11590:SF40; HEMOCYTE PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR Pfam; PF00927; Transglut_C; 2.
DR Pfam; PF01841; Transglut_core; 1.
DR Pfam; PF00868; Transglut_N; 1.
DR PIRSF; PIRSF000459; TGM_EBP42; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 428..521
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT ACT_SITE 436
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 495
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 518
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
SQ SEQUENCE 855 AA; 96874 MW; 60F3663F17C60163 CRC64;
MSSFDYHRQV FIAGIIHSAC LYKLVPLVRP LLHFGGLIAT PIFEHLRFIN NYDMIHPVDV
PVLFAERRQY LTSEIVESPS PLRRNAYGQC TSSAKLSRRV LPQVVLERGL ALWGNLFKET
SRFPVAIDER NEKDSQIRAD RLIFPDPVEP PTKKSPLELK LADLHIERNS ISHHTVDFNI
VQRDKDKKLV VRRGQPFEIS VSFYRDVDYE VDELKLVFEI GPQPTVANST KVVIILPLQE
GSNNRSAELW YAKVTKLEGK QLTIQINISP NCIVGRWNLK VVTYLKAAPR NEYLNSTSLI
SDVYVLFNPW NKNDMVFMPS EDLDEYVLND VGKIWRGSHS ALRPCYWSFG QFEDGILEAV
MNVLSRSSLP FPLCSNPIMV VRAMADMVQS PEGYSILEGD WAADYFTGTA PTEWTGSSRI
LQQYTKTGRQ ISYGHCWVFA GVMTTILRCL GIPTRIVTCY QAAHDSDKFV AVDIHVERNG
KLNKEGTQDK IWAFHVWNEC WMKRPDLPSS YSGWQVVDAT PQEKGDGITR VGPAPVRAIK
EGRLDIAYDT TNVISEVNAY KCYWVEDESG EEKLVEVVNE AIGLCISTKK PGRIFTGMNN
NDRLDITNQY KMSQESRDEV FNSLLPGHKA MISRYLMQKQ SEDVKFLFTM DDDVMLGEDF
HFEIVLTNLS DENRDINLSL RIESVHFSGR GNIKIKQEQI LLTIPPGRNH KYSSILHLND
YLSRSAGQFS FTAVVRIIVE QTGCVYIENR DFCAKMPNIN IVVSDALKVG KSSEVGLQFS
NPLPISLTGC KFIIEGPGIV ETLEVPCKKV SPRAIAKARC SVQPWRHGHD RILIAHFSSD
QLKDVDAAIA VDVNN
//